| Company Name: |
Hangzhou Go Top Peptide Biotech
|
| Tel: |
0571-88211921 13355716090 |
| Email: |
Sales@gotopbio.com |
| Products Intro: |
Product Name:Ghrelin
Purity:研发级，98%，HPLC，MS Package:1mg;10mg;100mg;1g;100g Remarks:60mg
|
|
| Product Name: | Ghrelin | | Synonyms: | Ghrelin | | CAS: | | | MF: | | | MW: | 0 | | EINECS: | | | Product Categories: | | | Mol File: | Mol File | ![Ghrelin Structure]() |
| | Ghrelin Chemical Properties |
| | Ghrelin Usage And Synthesis |
| Discovery | In 1999, Kojima et al. isolated GHRL from rat stomach
extracts by the orphan receptor strategy using the growth
hormone secretagogue receptor type-1a (GHS-R1a). The
name originates from its growth hormone-releasing
activity, with reference to the Proto-Indo-European word
“ghre,” meaning “grow,” and growth hormone release +in
(suffix of inducing) to give “ghrelin.” | | Structure | The serine residue at position 3 (Ser-3) is modified by
middle-chain fatty acids, and GHRL usually refers to the
octanoylated form (acylated ghrelin) . While
n-decanoic acid contributes to the modification, species
difference was seen. Only in the genus Rana (frogs) of
the anuran amphibian was acylated aa substituted from
Ser-3 to threonine. The first seven aa sequence
(GSSFLSP) is highly conserved across animal species.
Teleost GHRLs have an amide structure at the
C-terminus.The elasmobranch stingray GHRL has
O-glycosylation at Ser-10 and/or Thr-11 in addition to
the acylation at Ser-3. Mammalian GHRLs consist of 28 aa in general, but a
27-aa molecule lacking the 14th glutamine residue by
alternative splicing, namely des-Gln14 ghrelin, has also
been identified. Amino acid
sequences have been determined in nonmammalian vertebrates, including cartilaginous fish, bony
fish, amphibians, and reptiles
and birds. The number of aa ranges from
16 (stingray) to 28 residues (frogs) depending on the
species. | | Gene, mRNA, and precursor | The mRNA from the GHRL gene (chromosomal location: 3p25.3 for humans, 6 E3j6 52.84 cM for mice, and
4q42 for rats) codes for a 117-aa preproGHRL, consisting
of six exons (the presence of extended exon 0 and novel
exon -1 was found,5 thereby the composition of the
GHRL gene was reviewed). Mammalian
GHRL mRNAs are about 480–510 bp in length. The
prohormone convertase 1/3 (PC1/3) cleaves a 28-aa
unacylated ghrelin and a C-peptide in which a GHRL
gene-derived peptide, obestatin, is also cleaved from
proGHRL. Several natural antisense transcripts, termed ghrelinOS (ghrelin opposite strand) transcripts, are demonstrated. Semi et al. identified a novel human exon 2-deleted variant, and this splice variant and
intron 1-GHRL encode a C-terminally truncated form of
the GHRL peptide (GHRL1–13), termed miniGHRL. These
variants are present in humans, mice, and other nonmammalian vertebrates. | | Properties | Human GHRL: Mr 3371.9. Lyophilized material is stable at -30°C, but -80°C is more desirable. Soluble in
water. Because of high adsorptivity, it is desirable to
maintain the storage concentration at >10-4M, or to
dilute with saline containing 5% mannitol or 0.2% BSA
for treatment. | | Synthesis | Gastric GHRL expression increases by fasting, possibly through decreased plasma carbohydrates. In the rat
stomach or in thyroid removal, insulin or leptin stimulates and growth hormone (GH) treatment inhibits GHRL
gene expression. Expression in the rat stomach appears
from the first day after birth, and increases with age,
reaching a constant level around 40 days after birth.
Ghrelin-O-acyltransferase (GOAT) contributes to
acylation. | | Receptors | The ghrelin receptor (GHS-R1a) is a member of the
Class A GPCR family. The GHRL receptor gene
(GHSR), 3q26.31 in humans, comprises two exons and
one intron. Two isoforms, GHS-R1a and
GHS-R1b, exist in the same gene. GHS-R1a acts as a functional GHRL receptor,10 and GHS-R1b is a mRNA splicing variant that acts as a dominant negative mutant for
GHS-R1a. Human GHS-R1a and 1b have 366 aa and
289 aa, respectively. GHS-R1b lacks the
structure after TMD 5 of GHS-R1a, and 24 aa that originate from the intron sequence elongate after the 265th
leucine at the C-terminus of TMD 6. | | Biological functions | GHRL receptors are expressed in the hypothalamic
neuropeptide Y (NPY), somatostatin (SST), growth
hormone-releasing hormone (GHRH), proopiomelanocortin (POMC), orexin, and Agouti-related peptide
(AgRP) neurons in the pituitary, lung, heart, stomach,
intestine, pancreas, thymus, gonads, thyroid, kidney,
and adipose tissue. GHRL’s functions include stimulation of GH release, feeding, anxiety, learning and memory, gastrointestinal contraction, fat accumulation,
depression, gastric acid secretion, sleep duration, and
inhibition of drinking. Species differences are seen—
for example, feeding is stimulated in goldfish and frogs,
but inhibited in chickens and rainbow trout.MiniGHRL
appears to have similar actions to full-length GHRL, as
treatment with the exogenous miniGHRL peptide stimulates appetite and feeding in mice. Exon 2-deleted prepro GHRL overexpression stimulates the proliferation and
cell migration of the PC3 prostate cancer cell. | | Agonists and Antagonists | Des-Gln14-GHRL, [His1
, Lys6
]-GHRP-6, hexarelin,
D-Ala-β-[2-Nal]-D-Ala-Trp-D-Phe-Lys-amide (KP-102),
Aib-His-D-2-Nal-D-Phe-Lys-amide, wFw-Isn-amide,
L-692.585, capromorelin, tabimorelin, adenosin, anamorelin,
examorelin, ibutamoren, ipamorelin, macimorelin, pralmorelin, relamorelin, SM-103.686, teaghrelins, and ulimor. [D-Lys3]-GHRP-6, Cortistatin-8 [D-Arg1
, D-Phe5
,
D-Trp7,9, Leu11]-Substance P, YIL781, [D-Arg1
, D-Phe5
,
D-Trp7,9, Leu11]-Substance P, GSK1614343,
PF-05190457, BIM28163, YIL781, JMV3008, liverexpressing antimicrobial peptide-2(LEAP-2), and
Abbott14c. | | Clinical implications | In humans, an association between variations of the
GHRL gene and obesity has been suggested. GHRL gene
polymorphisms (604G/A, Arg51Gln, Leu72Met, and
Leu90Gln) seem to be associated with cardiovascular disease, carcinoma, type 2 diabetes, and Alzheimer’s disease.
There is a possibility that the Brachman-de Lange syndrome with poor growth occurs due to the overlap or
translocation of the chromosome on which the GHSR gene
is located. Furthermore, abnormal ghrelin responses
may play important roles in various GI disorders such
as chronic gastritis, Helicobacter pylori infection, irritable
bowel syndrome, functional dyspepsia, cachexia, celiac
disease, and inflammatory bowel disease. | | Description | A unique fatty acid modification mainly with n-octanoic
acid at the third serine residue of ghrelin is essential for eliciting ghrelin’s activity. Ghrelin is the first peripheral hormone
found to stimulate feeding behavior. Now, multiple functions
as hormonal secretagogues as well as lipid and glucose regulators have been demonstrated. | | Uses | The application of GHRL for treatments is still in at the
clinical trial stage. The expectation is that it might be
used as an appetite inducer, for treatment of GH deficiency and improvement of cardiac function, to stimulate
breathing in chronic obstructive pulmonary disease
(COPD), to stimulate gastrointestinal motility, and in
the treatment of obesity and type 2 diabetes. |
| | Ghrelin Preparation Products And Raw materials |
|